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313  structures 1457  species 0  interactions 51026  sequences 1546  architectures

Family: PHD (PF00628)

Summary: PHD-finger

Pfam includes annotations and additional family information from a range of different sources. These sources can be accessed via the tabs below.

This is the Wikipedia entry entitled "PHD finger". More...

PHD finger Edit Wikipedia article

PHD-finger
PDB 1f62 EBI.jpg
PHD zinc finger. Zinc atoms shown in grey
Identifiers
SymbolPHD
PfamPF00628
Pfam clanCL0390
InterProIPR019787
PROSITEPS50016
SCOPe1f62 / SUPFAM
OPM superfamily59
OPM protein1vfy

The PHD finger was discovered in 1993 as a Cys4-His-Cys3 motif in the plant homeodomain (hence PHD) proteins HAT3.1 in Arabidopsis thaliana and maize ZmHox1a.[1] The PHD finger motif resembles the metal binding RING domain (Cys3-His-Cys4) and FYVE domain. It occurs as a single finger, but often in clusters of two or three, and it also occurs together with other domains, such as the chromodomain and the bromodomain.

Role in epigenetics

The PHD finger, approximately 50-80 amino acids in length, is found in more than 100 human proteins. Several of the proteins it occurs in are found in the nucleus, and are involved in chromatin-mediated gene regulation. The PHD finger occurs in proteins such as the transcriptional co-activators p300 and CBP, Polycomb-like protein (Pcl), Trithorax-group proteins like ASH1L, ASH2L and MLL, the autoimmune regulator (AIRE), Mi-2 complex (part of histone deacetylase complex), the co-repressor TIF1, the JARID1-family of demethylases and many more.

Structure

The NMR structure of the PHD finger from human WSTF (Williams Syndrome Transcription Factor) shows that the conserved cysteines and histidine coordinate two Zn2+ ions. In general, the PHD finger adopts a globular fold, consisting of a two-stranded beta-sheet and an alpha-helix. The region consisting of these secondary structures and the residues involved in coordinating the zinc-ions are very conserved among species. The loop regions I and II are variable and could contribute functional specificity to the different PHD fingers.

Function

Recently the PHD fingers of some proteins, including ING2, YNG1 and NURF, have been reported to bind to histone H3 tri-methylated on lysine 4 (H3K4me3), while other PHD fingers have tested negative in such assays. A protein called SMCX (or JARID1C) has a PHD finger, which has been reported to bind histone H3 tri-methylated lysine 9 (H3K9me3). Based on these recent publications, binding to tri-methylated lysines on histones may therefore be a property widespread among PHD fingers. Domains that bind to modified histones, are called epigenetic readers as they specifically recognize the modified version of the residue and binds to it. The modification H3K4me3 is associated with the transcription start site of active genes, while H3K9me3 is associated with inactive genes. The modifications of the histone lysines are dynamic, as there are methylases that add methyl groups to the lysines, and there are demethylases that remove methyl groups. The SMCX protein is actually a histone H3 lysine 4 demethylase, which means it is an enzyme that can remove the methyl groups of lysine 4 on histone 3 (making it H3K4me2 or H3K4me1). One can only speculate if the H3K9me3-binding of SMCX PHD domain provides a crosstalk between trimethylation of H3K9 and the demethylation of H3K4me3. Such crosstalks have been suggested earlier with other domains involved in chromatin regulation, and may provide a strictly coordinated regulation.

Another example is the PHD finger of the BHC80/PHF21A protein, which is a component of the LSD1 complex. In this complex, LSD1 specifically demethylates H3K4me2 to H3K4me0, and BHC80 binds H3K4me0 through its PHD finger to stabilize the complex at its target promoters, presumably to prevent further re-methylation. This is the first example of a PHD finger recognizing lysine methyl-zero status.

References

  1. ^ Schindler U, Beckmann H, Cashmore AR (July 1993). "HAT3.1, a novel Arabidopsis homeodomain protein containing a conserved cysteine-rich region". The Plant Journal. 4 (1): 137–50. doi:10.1046/j.1365-313x.1993.04010137.x. PMID 8106082.

Further reading

This page is based on a Wikipedia article. The text is available under the Creative Commons Attribution/Share-Alike License.

This tab holds the annotation information that is stored in the Pfam database. As we move to using Wikipedia as our main source of annotation, the contents of this tab will be gradually replaced by the Wikipedia tab.

PHD-finger Provide feedback

PHD folds into an interleaved type of Zn-finger chelating 2 Zn ions in a similar manner to that of the RING and FYVE domains [2]. Several PHD fingers have been identified as binding modules of methylated histone H3 [3].

Literature references

  1. Aasland R, Gibson TJ, Stewart AF; , Trends Biochem Sci 1995;20:56-59.: The PHD finger: implications for chromatin-mediated transcriptional regulation. PUBMED:7701562 EPMC:7701562

  2. Pascual J, Martinez-Yamout M, Dyson HJ, Wright PE; , J Mol Biol 2000;304:723-729.: Structure of the PHD zinc finger from human williams-beuren syndrome transcription factor PUBMED:11124022 EPMC:11124022

  3. Shi X, Kachirskaia I, Walter KL, Kuo JH, Lake A, Davrazou F, Chan SM, Martin DG, Fingerman IM, Briggs SD, Howe L, Utz PJ, Kutateladze TG, Lugovskoy AA, Bedford MT, Gozani O; , J Biol Chem. 2006; [Epub ahead of print]: Proteome-wide analysis in S. cerevisiae identifies several PHD fingers as novel direct and selective binding modules of histone H3 methylated at either lysine 4 or lysine 36. PUBMED:17142463 EPMC:17142463


Internal database links

External database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR019787

Zinc finger (Znf) domains are relatively small protein motifs which contain multiple finger-like protrusions that make tandem contacts with their target molecule. Some of these domains bind zinc, but many do not; instead binding other metals such as iron, or no metal at all. For example, some family members form salt bridges to stabilise the finger-like folds. They were first identified as a DNA-binding motif in transcription factor TFIIIA from Xenopus laevis (African clawed frog), however they are now recognised to bind DNA, RNA, protein and/or lipid substrates [ PUBMED:10529348 , PUBMED:15963892 , PUBMED:15718139 , PUBMED:17210253 , PUBMED:12665246 ]. Their binding properties depend on the amino acid sequence of the finger domains and of the linker between fingers, as well as on the higher-order structures and the number of fingers. Znf domains are often found in clusters, where fingers can have different binding specificities. There are many superfamilies of Znf motifs, varying in both sequence and structure. They display considerable versatility in binding modes, even between members of the same class (e.g. some bind DNA, others protein), suggesting that Znf motifs are stable scaffolds that have evolved specialised functions. For example, Znf-containing proteins function in gene transcription, translation, mRNA trafficking, cytoskeleton organisation, epithelial development, cell adhesion, protein folding, chromatin remodelling and zinc sensing, to name but a few [ PUBMED:11179890 ]. Zinc-binding motifs are stable structures, and they rarely undergo conformational changes upon binding their target.

This entry represents the PHD (homeodomain) zinc finger domain [ PUBMED:7701562 ], which is a C4HC3 zinc-finger-like motif found in nuclear proteins thought to be involved in chromatin-mediated transcriptional regulation. The PHD finger motif is reminiscent of, but distinct from the C3HC4 type RING finger.

The function of this domain is not yet known but in analogy with the LIM domain it could be involved in protein-protein interaction and be important for the assembly or activity of multicomponent complexes involved in transcriptional activation or repression. Alternatively, the interactions could be intra-molecular and be important in maintaining the structural integrity of the protein. In similarity to the RING finger and the LIM domain, the PHD finger is thought to bind two zinc ions.

Domain organisation

Below is a listing of the unique domain organisations or architectures in which this domain is found. More...

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Pfam Clan

This family is a member of clan zf-FYVE-PHD (CL0390), which has the following description:

Superfamily contains a number of zinc-fingers, of the FYVE/PHD type, which are found in several groups of proteins including myelin-associated oligodendrocytic basic proteins (MOBP) Rabphilins, melanophilins, exophilins and myosin-VIIA and Rab-interacting protein families.

The clan contains the following 13 members:

ADD_ATRX ADD_DNMT3 FYVE FYVE_2 PHD PHD_2 PHD_4 PHD_Oberon RAG2_PHD zf-HC5HC2H zf-HC5HC2H_2 zf-PHD-like zf-piccolo

Alignments

We store a range of different sequence alignments for families. As well as the seed alignment from which the family is built, we provide the full alignment, generated by searching the sequence database (reference proteomes) using the family HMM. We also generate alignments using four representative proteomes (RP) sets and the UniProtKB sequence database. More...

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We make a range of alignments for each Pfam-A family. You can see a description of each above. You can view these alignments in various ways but please note that some types of alignment are never generated while others may not be available for all families, most commonly because the alignments are too large to handle.

  Seed
(71)
Full
(51026)
Representative proteomes UniProt
(89238)
RP15
(7103)
RP35
(20641)
RP55
(42655)
RP75
(58966)
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PP/heatmap 1            

1Cannot generate PP/Heatmap alignments for seeds; no PP data available

Key: ✓ available, x not generated, not available.

Format an alignment

  Seed
(71)
Full
(51026)
Representative proteomes UniProt
(89238)
RP15
(7103)
RP35
(20641)
RP55
(42655)
RP75
(58966)
Alignment:
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We make all of our alignments available in Stockholm format. You can download them here as raw, plain text files or as gzip-compressed files.

  Seed
(71)
Full
(51026)
Representative proteomes UniProt
(89238)
RP15
(7103)
RP35
(20641)
RP55
(42655)
RP75
(58966)
Raw Stockholm Download   Download   Download   Download   Download   Download   Download  
Gzipped Download   Download   Download   Download   Download   Download   Download  

You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.

HMM logo

HMM logos is one way of visualising profile HMMs. Logos provide a quick overview of the properties of an HMM in a graphical form. You can see a more detailed description of HMM logos and find out how you can interpret them here. More...

Trees

This page displays the phylogenetic tree for this family's seed alignment. We use FastTree to calculate neighbour join trees with a local bootstrap based on 100 resamples (shown next to the tree nodes). FastTree calculates approximately-maximum-likelihood phylogenetic trees from our seed alignment.

Note: You can also download the data file for the tree.

Curation and family details

This section shows the detailed information about the Pfam family. You can see the definitions of many of the terms in this section in the glossary and a fuller explanation of the scoring system that we use in the scores section of the help pages.

Curation View help on the curation process

Seed source: Prosite
Previous IDs: none
Type: Domain
Sequence Ontology: SO:0000417
Author: Pascual J , Bateman A
Number in seed: 71
Number in full: 51026
Average length of the domain: 50.00 aa
Average identity of full alignment: 30 %
Average coverage of the sequence by the domain: 5.61 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 57096847 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 28.9 28.9
Trusted cut-off 28.9 28.9
Noise cut-off 28.8 28.8
Model length: 52
Family (HMM) version: 31
Download: download the raw HMM for this family

Species distribution

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Structures

For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the PHD domain has been found. There are 313 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein sequence.

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AlphaFold Structure Predictions

The list of proteins below match this family and have AlphaFold predicted structures. Click on the protein accession to view the predicted structure.

Protein Predicted structure External Information
A0A0B4K6G3 View 3D Structure Click here
A0A0G2JTU9 View 3D Structure Click here
A0A0G2JTU9 View 3D Structure Click here
A0A0G2K175 View 3D Structure Click here
A0A0G2K426 View 3D Structure Click here
A0A0G2K426 View 3D Structure Click here
A0A0G2K6G9 View 3D Structure Click here
A0A0G2K6G9 View 3D Structure Click here
A0A0G2K6G9 View 3D Structure Click here
A0A0G2K7P2 View 3D Structure Click here
A0A0G2K7P2 View 3D Structure Click here
A0A0G2K897 View 3D Structure Click here
A0A0G2K948 View 3D Structure Click here
A0A0G2K948 View 3D Structure Click here
A0A0G2KR99 View 3D Structure Click here
A0A0G2KR99 View 3D Structure Click here
A0A0G2L648 View 3D Structure Click here
A0A0P0VB64 View 3D Structure Click here
A0A0P0VDJ3 View 3D Structure Click here
A0A0P0VE60 View 3D Structure Click here
A0A0P0VFU0 View 3D Structure Click here
A0A0P0W3M9 View 3D Structure Click here
A0A0P0WGU7 View 3D Structure Click here
A0A0P0X1A3 View 3D Structure Click here
A0A0P0X1F1 View 3D Structure Click here
A0A0P0XA66 View 3D Structure Click here
A0A0P0Y140 View 3D Structure Click here
A0A0R0EQU1 View 3D Structure Click here
A0A0R0FL58 View 3D Structure Click here
A0A0R0FQK5 View 3D Structure Click here
A0A0R0GFU6 View 3D Structure Click here
A0A0R0GMI8 View 3D Structure Click here
A0A0R0GMI8 View 3D Structure Click here
A0A0R0GV05 View 3D Structure Click here
A0A0R0H3K4 View 3D Structure Click here
A0A0R0HGS4 View 3D Structure Click here
A0A0R0HW95 View 3D Structure Click here
A0A0R0IJ30 View 3D Structure Click here
A0A0R0JA09 View 3D Structure Click here
A0A0R0JPU7 View 3D Structure Click here
A0A0R0JZR3 View 3D Structure Click here
A0A0R0K9Y0 View 3D Structure Click here
A0A0R0KU12 View 3D Structure Click here
A0A0R0KVA4 View 3D Structure Click here
A0A0R0L1U1 View 3D Structure Click here
A0A0R0L385 View 3D Structure Click here
A0A0R4IBT4 View 3D Structure Click here
A0A0R4IFV8 View 3D Structure Click here
A0A0R4IGC5 View 3D Structure Click here
A0A0R4IJ89 View 3D Structure Click here
A0A0R4IJ89 View 3D Structure Click here
A0A0R4ITE9 View 3D Structure Click here
A0A0R4IVN8 View 3D Structure Click here
A0A1D6EI69 View 3D Structure Click here
A0A1D6EW42 View 3D Structure Click here
A0A1D6F4U2 View 3D Structure Click here
A0A1D6FB17 View 3D Structure Click here
A0A1D6FXH3 View 3D Structure Click here
A0A1D6G3Z2 View 3D Structure Click here
A0A1D6G7C6 View 3D Structure Click here
A0A1D6G7M0 View 3D Structure Click here
A0A1D6GBR6 View 3D Structure Click here
A0A1D6GEK2 View 3D Structure Click here
A0A1D6GJ36 View 3D Structure Click here
A0A1D6GXC6 View 3D Structure Click here
A0A1D6GXC6 View 3D Structure Click here
A0A1D6GXJ5 View 3D Structure Click here
A0A1D6GYZ0 View 3D Structure Click here
A0A1D6HAX1 View 3D Structure Click here
A0A1D6HTA3 View 3D Structure Click here
A0A1D6I3R9 View 3D Structure Click here
A0A1D6I5L8 View 3D Structure Click here
A0A1D6IBX9 View 3D Structure Click here
A0A1D6IJA0 View 3D Structure Click here
A0A1D6IMF4 View 3D Structure Click here
A0A1D6IT56 View 3D Structure Click here
A0A1D6IWT6 View 3D Structure Click here
A0A1D6IX22 View 3D Structure Click here
A0A1D6J7E5 View 3D Structure Click here
A0A1D6J7E5 View 3D Structure Click here
A0A1D6JDZ1 View 3D Structure Click here
A0A1D6JZC0 View 3D Structure Click here
A0A1D6K064 View 3D Structure Click here
A0A1D6K5S8 View 3D Structure Click here
A0A1D6L4A5 View 3D Structure Click here
A0A1D6LQE4 View 3D Structure Click here
A0A1D6LTU1 View 3D Structure Click here
A0A1D6LYQ7 View 3D Structure Click here
A0A1D6MAU6 View 3D Structure Click here
A0A1D6MAV2 View 3D Structure Click here
A0A1D6MAV9 View 3D Structure Click here
A0A1D6MIQ2 View 3D Structure Click here
A0A1D6MXS1 View 3D Structure Click here
A0A1D6MY24 View 3D Structure Click here
A0A1D6N5E7 View 3D Structure Click here
A0A1D6NC34 View 3D Structure Click here
A0A1D6NTH3 View 3D Structure Click here
A0A1D6PC95 View 3D Structure Click here
A0A1D6PRB2 View 3D Structure Click here
A0A1D6PRK8 View 3D Structure Click here
A0A1D6Q3E8 View 3D Structure Click here
A0A1D6QRM7 View 3D Structure Click here
A0A1D6QU35 View 3D Structure Click here
A0A1D8PDM2 View 3D Structure Click here
A0A1D8PL24 View 3D Structure Click here
A0A1D8PQ51 View 3D Structure Click here
A0A1D8PR21 View 3D Structure Click here
A0A1D8PR21 View 3D Structure Click here
A0A1I9LNX5 View 3D Structure Click here
A0A1P8AP94 View 3D Structure Click here
A0A1P8B7I1 View 3D Structure Click here
A0A286Y9D1 View 3D Structure Click here
A0A286Y9D1 View 3D Structure Click here
A0A286Y9D1 View 3D Structure Click here
A0A2R8Q3B4 View 3D Structure Click here
A0A2R8Q3B4 View 3D Structure Click here
A0A2R8QBQ6 View 3D Structure Click here
A0A2R8QK64 View 3D Structure Click here
A0A2R8QQ41 View 3D Structure Click here
A0A2R8QRK9 View 3D Structure Click here
A0A2R8RUQ1 View 3D Structure Click here
A0A2R8RZL6 View 3D Structure Click here
A0A2R8RZL6 View 3D Structure Click here
A0A368UGE2 View 3D Structure Click here
A0A368UH09 View 3D Structure Click here
A0A368UIK8 View 3D Structure Click here
A0A368UJT0 View 3D Structure Click here
A1A5S2 View 3D Structure Click here
A2A8L1 View 3D Structure Click here
A2A8L1 View 3D Structure Click here
A2AUY4 View 3D Structure Click here
A2BIL7 View 3D Structure Click here
A2CG09 View 3D Structure Click here
A2CG09 View 3D Structure Click here
A5PF46 View 3D Structure Click here
A5PF46 View 3D Structure Click here
A6H619 View 3D Structure Click here
A8HAK1 View 3D Structure Click here
A9LMC0 View 3D Structure Click here
A9LMC0 View 3D Structure Click here
B0S6L0 View 3D Structure Click here
B0UXK0 View 3D Structure Click here
B1AR17 View 3D Structure Click here
B1AR17 View 3D Structure Click here
B2RQG2 View 3D Structure Click here
B4FCH3 View 3D Structure Click here
B4FK95 View 3D Structure Click here
B4FM57 View 3D Structure Click here
B5DFG8 View 3D Structure Click here
B6SV09 View 3D Structure Click here
B6SV09 View 3D Structure Click here
B6TK34 View 3D Structure Click here
B6U0S2 View 3D Structure Click here
B6U670 View 3D Structure Click here
B6UGC3 View 3D Structure Click here
B7ZUU3 View 3D Structure Click here
B8A483 View 3D Structure Click here
B8A5S8 View 3D Structure Click here
C0PCY4 View 3D Structure Click here
C0PIM9 View 3D Structure Click here
C0PIM9 View 3D Structure Click here
C4J6F2 View 3D Structure Click here
C6T2S0 View 3D Structure Click here
C6T7X8 View 3D Structure Click here
D3ZD32 View 3D Structure Click here
D3ZD32 View 3D Structure Click here
D3ZG56 View 3D Structure Click here
D3ZGQ8 View 3D Structure Click here
D3ZJ51 View 3D Structure Click here
D3ZK36 View 3D Structure Click here
D3ZKI5 View 3D Structure Click here
D3ZUK4 View 3D Structure Click here
D3ZV49 View 3D Structure Click here
D3ZWL9 View 3D Structure Click here
D4A9U0 View 3D Structure Click here
D4AD31 View 3D Structure Click here
E7EXI6 View 3D Structure Click here
E7EXI6 View 3D Structure Click here
E7EZF3 View 3D Structure Click here
E7F805 View 3D Structure Click here
E7FDQ1 View 3D Structure Click here
E9P861 View 3D Structure Click here
E9PU01 View 3D Structure Click here
E9PU01 View 3D Structure Click here
E9PWW9 View 3D Structure Click here
F1LM99 View 3D Structure Click here
F1LM99 View 3D Structure Click here
F1LMD5 View 3D Structure Click here
F1LPP8 View 3D Structure Click here
F1LPP8 View 3D Structure Click here
F1M1Y4 View 3D Structure Click here
F1M4U9 View 3D Structure Click here
F1M5T3 View 3D Structure Click here
F1M6K4 View 3D Structure Click here
F1M6Z0 View 3D Structure Click here
F1Q6Y6 View 3D Structure Click here
F1QD11 View 3D Structure Click here
F1QWV5 View 3D Structure Click here
F1QWV5 View 3D Structure Click here
F1QXL1 View 3D Structure Click here
F1RBT2 View 3D Structure Click here
F1RBT2 View 3D Structure Click here
F4IF36 View 3D Structure Click here
F4IQY0 View 3D Structure Click here
F4ISG1 View 3D Structure Click here
F4IXE7 View 3D Structure Click here
F4JL28 View 3D Structure Click here
F4JYC8 View 3D Structure Click here
F4K0Y2 View 3D Structure Click here
F4K4G6 View 3D Structure Click here
F4KBB1 View 3D Structure Click here
F4KBP5 View 3D Structure Click here
G3V661 View 3D Structure Click here
G5EBZ4 View 3D Structure Click here
G5EBZ4 View 3D Structure Click here
G5EGI1 View 3D Structure Click here
G5EGI1 View 3D Structure Click here
H0WEE0 View 3D Structure Click here
I1JAT7 View 3D Structure Click here
I1JLE1 View 3D Structure Click here
I1JY36 View 3D Structure Click here
I1JYS9 View 3D Structure Click here
I1K738 View 3D Structure Click here
I1K8P5 View 3D Structure Click here
I1KAR4 View 3D Structure Click here
I1KBH7 View 3D Structure Click here
I1KG14 View 3D Structure Click here
I1KH84 View 3D Structure Click here
I1KHV6 View 3D Structure Click here
I1KKF5 View 3D Structure Click here
I1KVW9 View 3D Structure Click here
I1L1N8 View 3D Structure Click here
I1L5S5 View 3D Structure Click here
I1LB70 View 3D Structure Click here
I1LC11 View 3D Structure Click here
I1LFT6 View 3D Structure Click here
I1LLM4 View 3D Structure Click here
I1LNQ5 View 3D Structure Click here
I1LPD8 View 3D Structure Click here
I1LQZ0 View 3D Structure Click here
I1LSW2 View 3D Structure Click here
I1LV46 View 3D Structure Click here
I1LVM1 View 3D Structure Click here
I1LY29 View 3D Structure Click here
I1M022 View 3D Structure Click here
I1M022 View 3D Structure Click here
I1M331 View 3D Structure Click here
I1M507 View 3D Structure Click here
I1M6L5 View 3D Structure Click here
I1M961 View 3D Structure Click here
I1MD29 View 3D Structure Click here
I1MDB1 View 3D Structure Click here
I1MI52 View 3D Structure Click here
I1MQU2 View 3D Structure Click here
I1N2Y0 View 3D Structure Click here
I1N521 View 3D Structure Click here
I1N5T6 View 3D Structure Click here
I1N5T6 View 3D Structure Click here
I1NID9 View 3D Structure Click here
K7K577 View 3D Structure Click here
K7K5J5 View 3D Structure Click here
K7K5X0 View 3D Structure Click here
K7KA70 View 3D Structure Click here
K7KGC4 View 3D Structure Click here
K7KHD4 View 3D Structure Click here
K7KIF9 View 3D Structure Click here
K7KPZ4 View 3D Structure Click here
K7KRW1 View 3D Structure Click here
K7KT35 View 3D Structure Click here
K7KUK8 View 3D Structure Click here
K7KUK8 View 3D Structure Click here
K7KWV8 View 3D Structure Click here
K7L425 View 3D Structure Click here
K7L4K0 View 3D Structure Click here
K7LC20 View 3D Structure Click here
K7LHF0 View 3D Structure Click here
K7LHQ9 View 3D Structure Click here
K7LLH5 View 3D Structure Click here
K7LMP3 View 3D Structure Click here
K7LN08 View 3D Structure Click here
K7LQ86 View 3D Structure Click here
K7LQW1 View 3D Structure Click here
K7LTR1 View 3D Structure Click here
K7LWG2 View 3D Structure Click here
K7LY35 View 3D Structure Click here
K7LY35 View 3D Structure Click here
K7M817 View 3D Structure Click here
K7M8N1 View 3D Structure Click here
K7MCR7 View 3D Structure Click here
K7MEU6 View 3D Structure Click here
K7MK01 View 3D Structure Click here
K7MK45 View 3D Structure Click here
K7MKK5 View 3D Structure Click here
K7MRE7 View 3D Structure Click here
K7N378 View 3D Structure Click here
K7N5B7 View 3D Structure Click here
K7TXX3 View 3D Structure Click here
M0R4T9 View 3D Structure Click here
O08629 View 3D Structure Click here
O15016 View 3D Structure Click here
O15164 View 3D Structure Click here
O16102 View 3D Structure Click here
O17006 View 3D Structure Click here
O43189 View 3D Structure Click here
O43918 View 3D Structure Click here
O44498 View 3D Structure Click here
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